2JZM
Chymotrypsin inhibitor C1 from Nicotiana alata
Summary for 2JZM
| Entry DOI | 10.2210/pdb2jzm/pdb |
| Descriptor | Proteinase inhibitor (1 entity in total) |
| Functional Keywords | protein, proteinase inhibitor, chymotrypsin inhibitor, plant, insecticidal, hydrolase inhibitor |
| Biological source | Nicotiana alata (Winged tobacco) |
| Total number of polymer chains | 1 |
| Total formula weight | 5746.48 |
| Authors | Schirra, H.J.,Anderson, M.A.,Craik, D.J. (deposition date: 2008-01-09, release date: 2008-11-25, Last modification date: 2019-10-09) |
| Primary citation | Schirra, H.J.,Anderson, M.A.,Craik, D.J. Structural refinement of insecticidal plant proteinase inhibitors from Nicotiana alata. Protein Pept.Lett., 15:903-909, 2008 Cited by PubMed Abstract: Ornamental tobacco (Nicotiana alata) produces a series of 6 kDa proteinase inhibitors belonging to the potato type II inhibitor family. These proteins inhibit trypsin and chymotrypsin, the main digestive enzymes of predatory insects, thus leading to starvation, impaired larval development or death. In this context, the three-dimensional structures of these inhibitors are important for developing novel strategies for pest control. The solution structures of C1 and T1, the two main prototypes of the N. alata inhibitors, were originally determined more than a decade ago (J. Mol. Biol. 242, 231-243 (1994) and Biochemistry 34, 14304-14311 (1995)). Since then methods for NMR structure calculations have evolved considerably. Here we report the refinement of the structures of C1 and T1 with state-of-the-art protocols for NMR structure calculations. This refinement leads to an improved quality of the structures, making them a more reliable basis for the development of novel pesticides and modeling applications. PubMed: 18991765DOI: 10.2174/092986608785849326 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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